4OIJ

X-ray crystal structure of racemic non-glycosylated chemokine Ser-CCL1

Summary for 4OIJ

• Entry DOI: 10.2210/pdb4oij/pdb
• Related: 4OIK
• Descriptor: C-C motif chemokine 1, D-Ser-CCL1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: chemical protein synthesis, racemic protein crystallography, glycoprotein, chemokine, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P22362
• Total number of polymer chains: 4
• Total formula weight: 37340.62

Authors

Okamoto, R.,Mandal, K.,Sawaya, M.R.,Kajihara, Y.,Yeates, T.O.,Kent, S.B.H. (deposition date: 2014-01-19, release date: 2014-05-07, Last modification date: 2024-11-20)

Primary citation

Okamoto, R.,Mandal, K.,Sawaya, M.R.,Kajihara, Y.,Yeates, T.O.,Kent, S.B.
(Quasi-)Racemic X-ray Structures of Glycosylated and Non-Glycosylated Forms of the Chemokine Ser-CCL1 Prepared by Total Chemical Synthesis.
Angew.Chem.Int.Ed.Engl., 53:5194-5198, 2014

PubMed Abstract: Our goal was to obtain the X-ray crystal structure of the glycosylated chemokine Ser-CCL1. Glycoproteins can be hard to crystallize because of the heterogeneity of the oligosaccharide (glycan) moiety. We used glycosylated Ser-CCL1 that had been prepared by total chemical synthesis as a homogeneous compound containing an N-linked asialo biantennary nonasaccharide glycan moiety of defined covalent structure. Facile crystal formation occurred from a quasi-racemic mixture consisting of glycosylated L-protein and non-glycosylated-D-protein, while no crystals were obtained from the glycosylated L-protein alone. The structure was solved at a resolution of 2.6-2.1 Å. However, the glycan moiety was disordered: only the N-linked GlcNAc sugar was well-defined in the electron density map. A racemic mixture of the protein enantiomers L-Ser-CCL1 and D-Ser-CCL1 was also crystallized, and the structure of the true racemate was solved at a resolution of 2.7-2.15 Å. Superimposition of the structures of the protein moieties of L-Ser-CCL1 and glycosylated-L-Ser-CCL1 revealed there was no significant alteration of the protein structure by N-glycosylation.

PubMed: 24692304
DOI: 10.1002/anie.201400679

Experimental method

X-RAY DIFFRACTION (2 Å)